Abstract

The structure of calmodulin and its specific interaction with several proteins will be examined, using a range of physical techniques. The molecular dynamics of calmodulin will be studied by measurements of the time decay of fluorescence anisotropy, as well as static anisotropy measurements, employing specifically located fluorescent probes. Particular attention will be paid to the effects of temperature and complex formation. The interaction of calmodulin with polypeptide hormones, troponin I, and myosin light chain kinase will be studied in detail. Radiationless energy transfer will be employed to investigate the spatial organization of complexes of calmodulin with other proteins.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases (NIADDK)
Type
Research Project (R01)
Project #
2R01AM030322-04
Application #
3152040
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1982-02-01
Project End
1990-01-31
Budget Start
1985-02-01
Budget End
1986-01-31
Support Year
4
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Maryland Balt CO Campus
Department
Type
Schools of Arts and Sciences
DUNS #
City
Baltimore
State
MD
Country
United States
Zip Code
21250

  Publications

Gryczynski, I; Lakowicz, J R; Steiner, R F (1988) Frequency-domain measurements of the rotational dynamics of the tyrosine groups of calmodulin. Biophys Chem 30:49-59
Caday, C G; Lambooy, P K; Steiner, R F (1986) The interaction of Ca2+-binding proteins with the carbocyanine dye stains-all. Biopolymers 25:1579-95
Caday, C G; Steiner, R F (1985) The interaction of calmodulin with the carbocyanine dye (Stains-all). J Biol Chem 260:5985-90
Campbell, B; Bucci, E; Steiner, R F (1985) Internal motions of band 3 of human erythrocytes. Biochemistry 24:4392-9